David Watson takes a digital sample of the water from Bear Creek on Oc. 18, 2014, in Aurora, Colorado. Metropolitan State University of Denver students and Groundworks Colorado are continuously taking samples of the water from Bear Creek, which has been seen to have high traces of E. coli, to help develop a plan to clean up the creek by 2020. (Photo By Brent Lewis/The Denver Post)

An accumulation of toxic amyloids In the body, associated with Parkinson’s disease, Alzheimer’s and other neurodegenerative diseases, might be inhibited by a protein in E. coli, a bacterium found in the human GI tract.

Amyloid is an abnormal protein usually produced in bone marrow that can be deposited in any tissue or organ. Clumps of these misfolded proteins can accumulate in the brain, damaging and killing cells and tissue.

The findings could point to a new therapeutic approach to Parkinson’s disease and a method for targeting amyloids associated with such neurodegenerative diseases.

E. coli make amyloid curli, the major proteinaceous component of a complex extracellular matrix produced by many in E. coli’s family of bacteria. E. coli makes amyloid curli on the cell surface, using them to attach the bacteria to surfaces such as intestinal walls or even bathroom sinks. The bacteria can cause serious infections.

The amyloids that E. coli produce do not form on the inside of the cell, where they would be toxic. Instead, they’re kept on the cell surface, where they’re helpful, necessary to the bacteria.

“It means that something in E. coli very specifically inhibits the assembly of the amyloid inside the cell. Therefore, amyloid formation only occurs outside the cell where it does not cause toxicity,” according to Margery Evans, a doctoral student in molecular, cellular, and developmental biology and lead author of the University of Michigan study.

Researchers uncovered a protein called CsgC that is a very specific, effective inhibitor of E. coli amyloid formation.

Amyloid is a class of fiber responsible for human diseases, including Alzheimer’s, Huntington’s, and prion diseases, although the process of amyloid formation is not well understood.

“Another implication of the research is that the curli could be a target for attacking biofilms, a kind of goo created by bacteria, which acts as a shield to thwart antibiotics and antiseptics,” Science Daily wrote of the research. “These bacteria can cause chronic infections, but treating these infections using molecules that block curli formation may degrade the biofilm and leave the bacteria more vulnerable to drug therapy.”

Electa Draper is the health writer for The Denver Post and has covered every news beat in a 22-year journalism career at three newspapers. She has a bachelor's degree in biology and a master's in journalism.